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3RRW

Crystal structure of the TL29 protein from Arabidopsis thaliana

3RRW の概要
エントリーDOI10.2210/pdb3rrw/pdb
分子名称Thylakoid lumenal 29 kDa protein, chloroplastic, PHOSPHATE ION, CALCIUM ION, ... (5 entities in total)
機能のキーワードchloroplast thylakoid lumen, plant protein
由来する生物種Arabidopsis thaliana (mouse-ear cress, thale-cress)
細胞内の位置Plastid, chloroplast thylakoid lumen : P82281
タンパク質・核酸の鎖数2
化学式量合計60026.42
構造登録者
Lundberg, E.,Storm, P.,Schroder, W.P.,Funk, C. (登録日: 2011-05-01, 公開日: 2011-08-03, 最終更新日: 2024-10-16)
主引用文献Lundberg, E.,Storm, P.,Schroder, W.P.,Funk, C.
Crystal structure of the TL29 protein from Arabidopsis thaliana: An APX homolog without peroxidase activity.
J.Struct.Biol., 176:24-31, 2011
Cited by
PubMed Abstract: TL29 is a plant-specific protein found in the thylakoid lumen of chloroplasts. Despite the putative requirement in plants for a peroxidase close to the site of photosynthetic oxygen production, and the sequence homology of TL29 to ascorbate peroxidases, so far biochemical methods have not shown this enzyme to possess peroxidase activity. Here we report the three-dimensional X-ray crystal structure of recombinant TL29 from Arabidopsis thaliana at a resolution of 2.5Å. The overall structure of TL29 is mainly alpha helical with six longer and six shorter helical segments. The TL29 structure resembles that of typical ascorbate peroxidases, however, crucial differences were found in regions that would be important for heme and ascorbate binding. Such differences suggest it to be highly unlikely that TL29 functions as a peroxidase.
PubMed: 21798352
DOI: 10.1016/j.jsb.2011.07.004
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 3rrw
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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